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The STRIPAK complex components FAM40A and FAM40B regulate endothelial cell contractility via ROCKs.

Narendra Suryavanshi1, Joanna Furmston1, Anne J Ridley2,3

  • 1Randall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, UK.

BMC Cell Biology
|December 5, 2018
PubMed
Summary
This summary is machine-generated.

The FAM40 proteins are crucial for endothelial cell function and vascular integrity. They interact with CCM3, impacting barrier permeability and angiogenesis, suggesting a role in cerebral cavernous malformations (CCM).

Keywords:
Actin cytoskeletonAdherens junctionsCerebral cavernous malformationsEndothelial cellsRho/ROCKSTRIPAK complex

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Area of Science:

  • Cell Biology
  • Vascular Biology
  • Protein Complexes

Background:

  • Endothelial cells form a regulated barrier between blood and tissues.
  • Cerebral cavernous malformations (CCM) involve dilated, leaky blood vessels, often linked to CCM3 mutations.
  • CCM3 is part of the STRIPAK protein complex, including FAM40A and FAM40B.

Purpose of the Study:

  • To investigate the interaction and function of FAM40A and FAM40B with CCM3.
  • To determine the role of FAM40 proteins in endothelial cell physiology and vascular integrity.

Main Methods:

  • RNA interference (RNAi) to deplete CCM3, FAM40A, or FAM40B in endothelial cells.
  • Assessment of stress fibers and in vitro angiogenesis (loop formation).
  • Measurement of endothelial permeability and inhibition of Rho-regulated ROCK kinases.

Main Results:

  • FAM40A and FAM40B interact with CCM3.
  • Depletion of CCM3, FAM40A, or FAM40B increased stress fibers and reduced angiogenesis.
  • FAM40B depletion increased endothelial permeability, effects reversible by ROCK kinase inhibition.

Conclusions:

  • FAM40 proteins are essential for endothelial cell function.
  • FAM40 proteins likely function within the CCM3-STRIPAK complex.
  • Dysregulation of FAM40 proteins may contribute to vascular pathologies like CCM.